N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) is an enzyme that catalyzes the production of uridine 5′-diphosphate-N-acetylglucosamine (hereinafter referred to as UDP-GlcNAc), an intermediate in biosynthesis of lipo-polysaccharides of gram-negative bacteria. Regarding GlmU polypeptides, the enzyme is purified from Escherichia coli, and it has been clarified that the enzyme catalyzes uridylation and also N-acetylation of glucosamine-1-phosphate [J. Bacteriol., 176, 6852 (1994)].
The glmU gene is obtained from bacteria of the genus Escherichia [J. Bacteriol., 175, 6150(1993)], those of the genus Bacillus [J. Bacteriol., 174, 6852 (1992)], those of the genus Streptococcus (Japanese Published Unexamined Patent Application No. 155582/1999), and those of the genus Neisseria [J. Bacteriol., 177, 6902 (1995)], but the glmU gene is not identified in bacteria of the genus Corynebacterium. 
It is reported that the N-acetylation activity of GlmU derived from Escherichia coli is unstable [J. Bacteriol., 176, 5788 (1994)], and the industrial application of the GlmU is problematic.
Regarding other bacteria from which the genes have been isolated, there is no description that suggests industrial production of GlmU polypeptides by the use of the gene.